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Volumn 135, Issue 4, 1996, Pages 965-980

Dictyostelium discoideum cells lacking the 34,000-dalton actin-binding protein can grow, locomote, and develop, but exhibit defects in regulation of cell structure and movement: A case of partial redundancy

Author keywords

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Indexed keywords

URIDINE PHOSPHATE;

EID: 0029828736     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.135.4.965     Document Type: Article
Times cited : (38)

References (94)
  • 1
    • 0025983823 scopus 로고
    • Requirement of yeast fimbrin for actin organization and morphogenesis in vivo
    • Adams, A.E.M., D. Botstein, and D.G. Drubin. 1991. Requirement of yeast fimbrin for actin organization and morphogenesis in vivo. Nature (Lond.). 354:404-408.
    • (1991) Nature (Lond.) , vol.354 , pp. 404-408
    • Adams, A.E.M.1    Botstein, D.2    Drubin, D.G.3
  • 2
    • 0024242826 scopus 로고
    • Isolation of an immunoreactive analog of brain fodrin that is associated with the cell cortex of Dictyostelium amoebae
    • Bennett, H., and J. Condeelis. 1988. Isolation of an immunoreactive analog of brain fodrin that is associated with the cell cortex of Dictyostelium amoebae. Cell Motil. Cytoskel. 11:303-317.
    • (1988) Cell Motil. Cytoskel. , vol.11 , pp. 303-317
    • Bennett, H.1    Condeelis, J.2
  • 3
    • 0015598482 scopus 로고
    • Dynamics of antigenic membrane sites relating to cell aggregation in Dictyostelium discoideum
    • Beug, H., F.E. Katz, and G. Gerisch. 1973. Dynamics of antigenic membrane sites relating to cell aggregation in Dictyostelium discoideum. J. Cell Biol. 56: 647-658.
    • (1973) J. Cell Biol. , vol.56 , pp. 647-658
    • Beug, H.1    Katz, F.E.2    Gerisch, G.3
  • 5
    • 0000167158 scopus 로고
    • Can genes be truly redundant?
    • Brookfield, J. 1992. Can genes be truly redundant? Curr. Biol. 2:553-554.
    • (1992) Curr. Biol. , vol.2 , pp. 553-554
    • Brookfield, J.1
  • 6
    • 0022328478 scopus 로고
    • A calcium insensitive actin-crosslinking protein from Dictyosteliurn discoideum
    • Brown, S.S. 1985. A calcium insensitive actin-crosslinking protein from Dictyosteliurn discoideum. Cell Motil. 5:529-543.
    • (1985) Cell Motil. , vol.5 , pp. 529-543
    • Brown, S.S.1
  • 7
    • 0029993426 scopus 로고    scopus 로고
    • Single amino acid mutations in Drosophila fascin disrupt actin bundling function in vivo
    • Cant, K., and L. Cooley. 1996. Single amino acid mutations in Drosophila fascin disrupt actin bundling function in vivo. Genetics. 143:249-258.
    • (1996) Genetics , vol.143 , pp. 249-258
    • Cant, K.1    Cooley, L.2
  • 8
    • 0028269631 scopus 로고
    • Drosophila singed, a fascin homolog, is required for actin bundle formation during oogenesis and bristle extension
    • Cant, K., B.A. Knowles, M.S. Mooseker, and L. Cooley. 1994. Drosophila singed, a fascin homolog, is required for actin bundle formation during oogenesis and bristle extension. J. Cell Biol. 125:369-380.
    • (1994) J. Cell Biol. , vol.125 , pp. 369-380
    • Cant, K.1    Knowles, B.A.2    Mooseker, M.S.3    Cooley, L.4
  • 10
    • 0021876405 scopus 로고
    • Ligand-induced changes in the location of actin, myosin, 95 k (α-actinin), and 120 k protein in amoebae of Dictyostelium discoideum
    • Carboni, J.M., and J.S. Condeelis. 1985. Ligand-induced changes in the location of actin, myosin, 95 k (α-actinin), and 120 k protein in amoebae of Dictyostelium discoideum. J. Cell Biol. 100:1894-1993.
    • (1985) J. Cell Biol. , vol.100 , pp. 1894-1993
    • Carboni, J.M.1    Condeelis, J.S.2
  • 11
    • 0027976354 scopus 로고
    • Mutation of the third intracellular loop of the cAMP receptor, cAR1, of Dictyostelium yields mutants impaired in multiple signaling pathways
    • Caterina, M.J., J.L.S. Milne, and P.N. Devreotes. 1994. Mutation of the third intracellular loop of the cAMP receptor, cAR1, of Dictyostelium yields mutants impaired in multiple signaling pathways. J. Biol. Chem. 269:1523-1532.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1523-1532
    • Caterina, M.J.1    Milne, J.L.S.2    Devreotes, P.N.3
  • 13
    • 0019499820 scopus 로고
    • A new protein that gels F-actin in the cell cortex of Dictyostelium discoideum
    • Condeelis, J., J. Salisbury, and K. Fujiwara. 1981. A new protein that gels F-actin in the cell cortex of Dictyostelium discoideum. Nature (Lond.). 292:161-163.
    • (1981) Nature (Lond.) , vol.292 , pp. 161-163
    • Condeelis, J.1    Salisbury, J.2    Fujiwara, K.3
  • 14
    • 0019975940 scopus 로고
    • A calcium and pH-regulated protein from Dictyostelium discoideum that cross-links filaments
    • Condeelis, J.S., and M. Vahey. 1982. A calcium and pH-regulated protein from Dictyostelium discoideum that cross-links filaments. J. Cell Biol. 94:466-471.
    • (1982) J. Cell Biol. , vol.94 , pp. 466-471
    • Condeelis, J.S.1    Vahey, M.2
  • 15
    • 0026570396 scopus 로고
    • Targeted disruption of the ABP-120 gene leads to cells with altered motility
    • Cox, D., J. Condeelis, D. Wessels, D. Soll, H. Kern, and D.A. Knecht. 1992. Targeted disruption of the ABP-120 gene leads to cells with altered motility. J. Cell Biol. 116:943-951
    • (1992) J. Cell Biol. , vol.116 , pp. 943-951
    • Cox, D.1    Condeelis, J.2    Wessels, D.3    Soll, D.4    Kern, H.5    Knecht, D.A.6
  • 16
    • 0028919541 scopus 로고
    • Genetic deletion of ABP-120 alters the three dimensional organization of actin filaments in Dictyostelium pseudopods
    • Cox, D., J.A. Ridsdale, J. Condeelis, and J. Hartwig. 1995. Genetic deletion of ABP-120 alters the three dimensional organization of actin filaments in Dictyostelium pseudopods. J. Cell Biol. 128:819-835.
    • (1995) J. Cell Biol. , vol.128 , pp. 819-835
    • Cox, D.1    Ridsdale, J.A.2    Condeelis, J.3    Hartwig, J.4
  • 17
    • 0029920367 scopus 로고    scopus 로고
    • Re-expression of ABP-120 rescues cytoskeletal, motilily, and phagocytosis defects of ABP-120 Dictyostelium mutants
    • Cox, D., D. Wessels, D.R. Soll, J. Hartwig, and J. Condeelis. 1996. Re-expression of ABP-120 rescues cytoskeletal, motilily, and phagocytosis defects of ABP-120 Dictyostelium mutants. Mol. Biol. Cell. 7:803-823.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 803-823
    • Cox, D.1    Wessels, D.2    Soll, D.R.3    Hartwig, J.4    Condeelis, J.5
  • 19
    • 0027389812 scopus 로고
    • Dictyostelium mutants lacking the cytoskeletal protein coronin are defective in cytokinesis and cell motility
    • de Hostos, E.L., C. Rehfuess, B. Bradtke, D.R. Waddell, R. Albrecht, J. Murphy, and G. Gerisch. 1993. Dictyostelium mutants lacking the cytoskeletal protein coronin are defective in cytokinesis and cell motility. J. Cell Biol. 120:163-173.
    • (1993) J. Cell Biol. , vol.120 , pp. 163-173
    • De Hostos, E.L.1    Rehfuess, C.2    Bradtke, B.3    Waddell, D.R.4    Albrecht, R.5    Murphy, J.6    Gerisch, G.7
  • 20
    • 0023250545 scopus 로고
    • Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination
    • De Lozanne, A., and J.A. Spudich. 1987. Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination. Science (Wash. DC). 236:1086-1091.
    • (1987) Science (Wash. DC) , vol.236 , pp. 1086-1091
    • De Lozanne, A.1    Spudich, J.A.2
  • 21
    • 0025002846 scopus 로고
    • Isolation of an abundant 50,000 dalton actin filament bundling protein from Dictyostelium discoideum
    • Demma, M., V. Warren, R. Hock, S. Dharmawardhane, and J. Condeelis. 1990. Isolation of an abundant 50,000 dalton actin filament bundling protein from Dictyostelium discoideum. J. Biol. Chem. 265:2286-2291.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2286-2291
    • Demma, M.1    Warren, V.2    Hock, R.3    Dharmawardhane, S.4    Condeelis, J.5
  • 22
    • 0024066415 scopus 로고
    • Structural characterization of Dictyostelium discoideum prespore-specific gene D19 and of its product, cell surface glycoprotein PsA
    • Early, A.E., J.G. Williams, H.E. Meyer, S.B. Por, E. Smith, K.L. Williams, and A.A. Gooley. 1988. Structural characterization of Dictyostelium discoideum prespore-specific gene D19 and of its product, cell surface glycoprotein PsA. Mol. Cell. Biol. 8:3458-3466.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3458-3466
    • Early, A.E.1    Williams, J.G.2    Meyer, H.E.3    Por, S.B.4    Smith, E.5    Williams, K.L.6    Gooley, A.A.7
  • 23
    • 0029020353 scopus 로고
    • pH regulation of the F-actin binding properties of Dictyostelium elongation factor 1-α
    • Edmonds, B.T., J. Murray, and J. Condeelis. 1995. pH regulation of the F-actin binding properties of Dictyostelium elongation factor 1-α. J. Biol. Chem. 270: 15222-15230.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15222-15230
    • Edmonds, B.T.1    Murray, J.2    Condeelis, J.3
  • 24
    • 0024671747 scopus 로고
    • Hygromycin resistance as a selectable marker in Dictyostelium discoideum
    • Egelhoff, T.T., S.S. Brown, D.J. Manstein, and J.A. Spudich. 1989. Hygromycin resistance as a selectable marker in Dictyostelium discoideum. Mol. Cell. Biol. 9:1965-1968.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1965-1968
    • Egelhoff, T.T.1    Brown, S.S.2    Manstein, D.J.3    Spudich, J.A.4
  • 25
    • 0027446459 scopus 로고
    • Gene knockouts of c-src, transforming growth factor β1, and tenascin suggest superfluous, nonfunctional expression of proteins
    • Erickson, H.P. 1993. Gene knockouts of c-src, transforming growth factor β1, and tenascin suggest superfluous, nonfunctional expression of proteins. J. Cell Biol. 120:1079-1081.
    • (1993) J. Cell Biol. , vol.120 , pp. 1079-1081
    • Erickson, H.P.1
  • 26
    • 0026650509 scopus 로고
    • Overexpression of the csA cell adhesion molecule under its own cAMP-regulated promoter impairs morphogenesis in Dictyostelium discoideum
    • Faix, J., G. Gerisch, and A.A. Noegel. 1992. Overexpression of the csA cell adhesion molecule under its own cAMP-regulated promoter impairs morphogenesis in Dictyostelium discoideum. J. Cell Sci. 102:203-214.
    • (1992) J. Cell Sci. , vol.102 , pp. 203-214
    • Faix, J.1    Gerisch, G.2    Noegel, A.A.3
  • 27
    • 0020414413 scopus 로고
    • A calcium and pH regulated actin binding protein from D. discoideum
    • Fechheimer, M., J. Brier, M. Rockwell, E.J. Luna, and D.L. Taylor. 1982. A calcium and pH regulated actin binding protein from D. discoideum. Cell Motil. 2:287-308.
    • (1982) Cell Motil. , vol.2 , pp. 287-308
    • Fechheimer, M.1    Brier, J.2    Rockwell, M.3    Luna, E.J.4    Taylor, D.L.5
  • 28
    • 0021759450 scopus 로고
    • Isolation and characterization of a 30,000-dalton calcium-sensitive actin crosslinking protein from Dictyostelium discoideum
    • Fechhcimer, M., and D.L. Taylor. 1984. Isolation and characterization of a 30,000-dalton calcium-sensitive actin crosslinking protein from Dictyostelium discoideum. J. Biol. Chem. 259:4514-4520.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4514-4520
    • Fechhcimer, M.1    Taylor, D.L.2
  • 29
    • 0023188266 scopus 로고
    • The Dictyostelium discoideum 30,000 dalton calcium-sensitive actin-bundling protein is selectively present in filopodia
    • Fechheimer, M. 1987. The Dictyostelium discoideum 30,000 dalton calcium-sensitive actin-bundling protein is selectively present in filopodia. J. Cell Biol. 104:1539-1551.
    • (1987) J. Cell Biol. , vol.104 , pp. 1539-1551
    • Fechheimer, M.1
  • 30
    • 0025727170 scopus 로고
    • Isolation and sequencing of cDNA clones encoding the Dictyostelium discoideum 30,000 dalton actin-bundling protein
    • Fechheimer, M., D. Murdock, M. Carney, and C.V.C. Glover. 1991. Isolation and sequencing of cDNA clones encoding the Dictyostelium discoideum 30,000 dalton actin-bundling protein. J. Biol. Chem. 266:2883-2889.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2883-2889
    • Fechheimer, M.1    Murdock, D.2    Carney, M.3    Glover, C.V.C.4
  • 31
    • 10544238750 scopus 로고
    • r <35,000) actin crosslinking proteins
    • T.E. Kreis and R.D. Vale, editors. Oxford University Press, Oxford, U.K.
    • r <35,000) actin crosslinking proteins. In Guidebook to the Cytoskeletal and Motor Proleins. T.E. Kreis and R.D. Vale, editors. Oxford University Press, Oxford, U.K. 74-76.
    • (1993) Guidebook to the Cytoskeletal and Motor Proleins , pp. 74-76
    • Fechheimer, M.1
  • 32
    • 0028022792 scopus 로고
    • Association of the Dictyostelium 30,000 dalton actin bundling protein with contact regions
    • Fechheimer, M., H.M. Ingalls, R. Furukawa, and E.J. Luna. 1994. Association of the Dictyostelium 30,000 dalton actin bundling protein with contact regions. J. Cell Sci. 107:2393-2401.
    • (1994) J. Cell Sci. , vol.107 , pp. 2393-2401
    • Fechheimer, M.1    Ingalls, H.M.2    Furukawa, R.3    Luna, E.J.4
  • 33
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg, A.P., and B. Vogelstein. 1983. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132:6-13.
    • (1983) Anal. Biochem. , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 34
    • 0024635815 scopus 로고
    • Quantitative analysis of cell motility and chemolaxis in Dictyostelium discoideum by using an image processing system and a novel chemotaxis chamber providing stationary chemical gradients
    • Fisher, P.R., R. Merkl, and G. Gerisch. 1989. Quantitative analysis of cell motility and chemolaxis in Dictyostelium discoideum by using an image processing system and a novel chemotaxis chamber providing stationary chemical gradients. J. Cell Biol. 108:973-984.
    • (1989) J. Cell Biol. , vol.108 , pp. 973-984
    • Fisher, P.R.1    Merkl, R.2    Gerisch, G.3
  • 35
    • 0017493805 scopus 로고
    • A defined minimal medium for axenic strains of Dictyostelium discoideum
    • Franke, J., and R. Kessin. 1977. A defined minimal medium for axenic strains of Dictyostelium discoideum. Proc. Natl. Acad. Sci. USA. 74:2157-2161.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 2157-2161
    • Franke, J.1    Kessin, R.2
  • 36
    • 0025637073 scopus 로고
    • Localization, expression, evolutionary conservation, and structure of the 30,000 dalton actin bundling protein of Dictyostelium discoideum
    • Furukawa, R., and M. Fechheimer. 1990. Localization, expression, evolutionary conservation, and structure of the 30,000 dalton actin bundling protein of Dictyostelium discoideum. Dev. Genet. 11:362-368.
    • (1990) Dev. Genet. , vol.11 , pp. 362-368
    • Furukawa, R.1    Fechheimer, M.2
  • 37
    • 0002036804 scopus 로고
    • The Dictyostelium discoideum 30,000 dalton protein contributes to phagocytosis
    • Furukawa, R., S. Butz, E. Fleischmann, and M. Fechheimer. 1992. The Dictyostelium discoideum 30,000 dalton protein contributes to phagocytosis. Protoplasma. 169:18-27.
    • (1992) Protoplasma , vol.169 , pp. 18-27
    • Furukawa, R.1    Butz, S.2    Fleischmann, E.3    Fechheimer, M.4
  • 38
    • 0028169756 scopus 로고
    • Differential localization of α-actinin and the 30 kD actin-bundling protein in the cleavage furrow, phagocytic cup, and contractile vacuole of Dictyostelium discoideum
    • Furukawa, R., and M. Fechheimer. 1994. Differential localization of α-actinin and the 30 kD actin-bundling protein in the cleavage furrow, phagocytic cup, and contractile vacuole of Dictyostelium discoideum. Cell Motil. Cytoskel. 29:46-56.
    • (1994) Cell Motil. Cytoskel. , vol.29 , pp. 46-56
    • Furukawa, R.1    Fechheimer, M.2
  • 40
    • 0028004565 scopus 로고
    • Dictyostelium amebas that lack G-actin sequestering profilins show defects in F-actin content, cytokinesis, and development
    • Haugwitz, M., A.A. Noegel, J. Karakesisoglou, and M. Schleicher. 1994. Dictyostelium amebas that lack G-actin sequestering profilins show defects in F-actin content, cytokinesis, and development. Cell. 79:303-314.
    • (1994) Cell , vol.79 , pp. 303-314
    • Haugwitz, M.1    Noegel, A.A.2    Karakesisoglou, J.3    Schleicher, M.4
  • 41
    • 0023091904 scopus 로고
    • Isolation of 240-kilodalton actin-binding protein from Dictyostelium discoideum
    • Hock, R.S., and J.S. Condeelis. 1987. Isolation of 240-kilodalton actin-binding protein from Dictyostelium discoideum. J. Biol. Chem. 262:394-400.
    • (1987) J. Biol. Chem. , vol.262 , pp. 394-400
    • Hock, R.S.1    Condeelis, J.S.2
  • 42
    • 0023968066 scopus 로고
    • Sequence analysis of the DdPyr5-6 gene coding for UMP synthase in Dictyostelium discoideum and comparison with orotate phosphoribosyl transferases and OMP decarboxylases
    • Jacquet, M., R. Guilbaud, and H. Garreau. 1988. Sequence analysis of the DdPyr5-6 gene coding for UMP synthase in Dictyostelium discoideum and comparison with orotate phosphoribosyl transferases and OMP decarboxylases. Mol. Gen. Genet. 211:441-445.
    • (1988) Mol. Gen. Genet. , vol.211 , pp. 441-445
    • Jacquet, M.1    Guilbaud, R.2    Garreau, H.3
  • 43
    • 0025871812 scopus 로고
    • Modulation of contraction by gelation/solation in a reconstituted motile model
    • Janson, L.W., J. Kolega, and D.L. Taylor. 1991. Modulation of contraction by gelation/solation in a reconstituted motile model. J. Cell Biol. 114:1005-1015.
    • (1991) J. Cell Biol. , vol.114 , pp. 1005-1015
    • Janson, L.W.1    Kolega, J.2    Taylor, D.L.3
  • 45
    • 0023203497 scopus 로고
    • Two distinct classes of prestalk-enriched mRNA sequences in Dictyostelium discoideum
    • Jermyn, K.A., M. Berks, R.R. Kay, and J.E. Williams. 1987. Two distinct classes of prestalk-enriched mRNA sequences in Dictyostelium discoideum. Development (Camb.). 100:745-755.
    • (1987) Development (Camb.) , vol.100 , pp. 745-755
    • Jermyn, K.A.1    Berks, M.2    Kay, R.R.3    Williams, J.E.4
  • 46
    • 0023742179 scopus 로고
    • Colocalization of F-actin and 34-kilodalton actin bundling protein in Dictyostelium and cultured fibroblasts
    • Johns, J.A., A.M. Brock, and J.D. Pardee. 1988. Colocalization of F-actin and 34-kilodalton actin bundling protein in Dictyostelium and cultured fibroblasts. Cell Motil. Cytoskel. 9:205-218.
    • (1988) Cell Motil. Cytoskel. , vol.9 , pp. 205-218
    • Johns, J.A.1    Brock, A.M.2    Pardee, J.D.3
  • 48
    • 0022815791 scopus 로고
    • Developmental regulation of Dictyostelium discoideum actin gene fusions carried on low-copy and high-copy transformation vectors
    • Knecht, D.A., S.M. Cohen, W.F. Loomis, and H.F. Lodish. 1986. Developmental regulation of Dictyostelium discoideum actin gene fusions carried on low-copy and high-copy transformation vectors. Mol. Cell. Biol. 6:3973-3983.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 3973-3983
    • Knecht, D.A.1    Cohen, S.M.2    Loomis, W.F.3    Lodish, H.F.4
  • 49
    • 0023189474 scopus 로고
    • Antisense RNA inactivation of myosin heavy chain gene expression in Dictyostelium discoideum
    • Knecht, D.A., and W.F. Loomis. 1987. Antisense RNA inactivation of myosin heavy chain gene expression in Dictyostelium discoideum. Science (Wash. DC). 241:1081-1086.
    • (1987) Science (Wash. DC) , vol.241 , pp. 1081-1086
    • Knecht, D.A.1    Loomis, W.F.2
  • 50
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 51
    • 0023663065 scopus 로고
    • Clathrin requirement for normal growth of yeast
    • Lemmon, S.K., and E.W. Jones. 1987. Clathrin requirement for normal growth of yeast. Science (Wash. DC). 238:504-509.
    • (1987) Science (Wash. DC) , vol.238 , pp. 504-509
    • Lemmon, S.K.1    Jones, E.W.2
  • 52
    • 0015012497 scopus 로고
    • Sensitivity of Dictyostelium discoideum to nucleic acid analogues
    • Loomis, W.F. 1971. Sensitivity of Dictyostelium discoideum to nucleic acid analogues. Exp. Cell Res. 64:484-486.
    • (1971) Exp. Cell Res. , vol.64 , pp. 484-486
    • Loomis, W.F.1
  • 53
    • 0031044473 scopus 로고    scopus 로고
    • Dynamic imaging of neutrophil migration in three dimensions: Mechanical interactions between cells and matrix
    • In press
    • Mandeville, J.T.H., M.A. Lawson, and F.R. Maxfield. 1997. Dynamic imaging of neutrophil migration in three dimensions: mechanical interactions between cells and matrix. J. Leukocyte Biol. In press.
    • (1997) J. Leukocyte Biol.
    • Mandeville, J.T.H.1    Lawson, M.A.2    Maxfield, F.R.3
  • 55
    • 0026034515 scopus 로고
    • Modular organization of actin crosslinking proteins
    • Matsudaira, P. 1991. Modular organization of actin crosslinking proteins. Trends Biochem. Sci. 16:87-92.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 87-92
    • Matsudaira, P.1
  • 56
    • 0014595592 scopus 로고
    • Alternative developmental pathways determined by environmental conditions in the cellular slime mold Dictyostelium discoideum
    • Newell, P.C., A. Telser, and M. Sussmann. 1969. Alternative developmental pathways determined by environmental conditions in the cellular slime mold Dictyostelium discoideum. J. Bacteriol. 100:763-768.
    • (1969) J. Bacteriol. , vol.100 , pp. 763-768
    • Newell, P.C.1    Telser, A.2    Sussmann, M.3
  • 57
    • 0005956187 scopus 로고
    • Developmentally regulated transcription of Dictyostelium discoideum plasmid Ddp1
    • Noegel, A.A., B.A. Metz, and K.L. Williams. 1985. Developmentally regulated transcription of Dictyostelium discoideum plasmid Ddp1. EMBO (Eur. Mol. Biol. Organ.) J. 4:3797-3803.
    • (1985) EMBO (Eur. Mol. Biol. Organ.) J. , vol.4 , pp. 3797-3803
    • Noegel, A.A.1    Metz, B.A.2    Williams, K.L.3
  • 58
    • 0023653358 scopus 로고
    • Calcium-sensitive non-muscle α-actinin contains EF-hand structures and highly conserved regions
    • Noegel, A., W. Witke, and M. Schleicher. 1987. Calcium-sensitive non-muscle α-actinin contains EF-hand structures and highly conserved regions. FEBS Lett. 221:391-396.
    • (1987) FEBS Lett. , vol.221 , pp. 391-396
    • Noegel, A.1    Witke, W.2    Schleicher, M.3
  • 59
    • 0024335961 scopus 로고
    • The Dictyostelium gelation factor shares a putative actin-binding site with α-actinin and dystrophin and also has a rod domain containing six 100 residue motifs that appear to have a cross-β conformation
    • Noegel, A., S. Rapp, F. Lottspeich, M. Schleicher, and M. Stewart. 1989. The Dictyostelium gelation factor shares a putative actin-binding site with α-actinin and dystrophin and also has a rod domain containing six 100 residue motifs that appear to have a cross-β conformation. J. Cell Biol. 108:607-618.
    • (1989) J. Cell Biol. , vol.108 , pp. 607-618
    • Noegel, A.1    Rapp, S.2    Lottspeich, F.3    Schleicher, M.4    Stewart, M.5
  • 60
    • 0028860154 scopus 로고
    • Differential association of three actin-bundling proteins with microfilaments in Dictyostelium amebas
    • Okazaki, K., and S. Yumura. 1995. Differential association of three actin-bundling proteins with microfilaments in Dictyostelium amebas. Eur. J. Cell Biol. 66:75-81.
    • (1995) Eur. J. Cell Biol. , vol.66 , pp. 75-81
    • Okazaki, K.1    Yumura, S.2
  • 61
    • 0029993449 scopus 로고    scopus 로고
    • Know your neighbors: Three phenotypes in null mutants of the myogenic bHLH gene MRF4
    • Oison, E.N., H.-H. Arnold, P.W.J. Rigby, and B.J. Wold. 1996. Know your neighbors: three phenotypes in null mutants of the myogenic bHLH gene MRF4. Cell. 85:1-4.
    • (1996) Cell , vol.85 , pp. 1-4
    • Oison, E.N.1    Arnold, H.-H.2    Rigby, P.W.J.3    Wold, B.J.4
  • 62
    • 0029987840 scopus 로고    scopus 로고
    • Overlapping functions of myosin-I isoforms?
    • Ostap, E.M., and T.D. Pollard. 1996. Overlapping functions of myosin-I isoforms? J. Cell Biol. 133:221-224.
    • (1996) J. Cell Biol. , vol.133 , pp. 221-224
    • Ostap, E.M.1    Pollard, T.D.2
  • 63
    • 0028140561 scopus 로고
    • Actin-bundling proteins
    • Otto, J.J. 1994. Actin-bundling proteins. Curr. Opin. Cell Biol. 6:105-109.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 105-109
    • Otto, J.J.1
  • 64
    • 0029859177 scopus 로고    scopus 로고
    • The role of the cortical cytoskeleton: F-actin cross-linking proteins protect against osmotic stress, ensure cell size, cell shape and motility, and contribute to phagocytosis and development
    • In press
    • Rivero, F., B. Koppel, B. Peracino, S. Bozzaro, F. Siegert, C.J. Weijer, M. Schleicher, R. Albrecht, and A.A. Noegel. 1996. The role of the cortical cytoskeleton: F-actin cross-linking proteins protect against osmotic stress, ensure cell size, cell shape and motility, and contribute to phagocytosis and development. J. Cell Sci. In press.
    • (1996) J. Cell Sci.
    • Rivero, F.1    Koppel, B.2    Peracino, B.3    Bozzaro, S.4    Siegert, F.5    Weijer, C.J.6    Schleicher, M.7    Albrecht, R.8    Noegel, A.A.9
  • 66
    • 0023091231 scopus 로고
    • Dependence of the mechanical properties of actin/alpha-actinin gels on deformation rate
    • Sato, M., W.H. Schwartz, and T.D. Pollard. 1987. Dependence of the mechanical properties of actin/alpha-actinin gels on deformation rate. Nature (Lond.). 325:828-830.
    • (1987) Nature (Lond.) , vol.325 , pp. 828-830
    • Sato, M.1    Schwartz, W.H.2    Pollard, T.D.3
  • 67
    • 0028929442 scopus 로고
    • Cell-substrate interactions and locomotion of Dictyostelium wild-type and mutants defective in three cytoskeletal proteins: A study using quantitative reflection interference contrast microscopy
    • Schindl, M., E. Wallraff, B. Deubzer, W. Witke, G. Gerisch, and E. Sackmann. 1995. Cell-substrate interactions and locomotion of Dictyostelium wild-type and mutants defective in three cytoskeletal proteins: a study using quantitative reflection interference contrast microscopy. Biophys. J. 68:1177-1190.
    • (1995) Biophys. J. , vol.68 , pp. 1177-1190
    • Schindl, M.1    Wallraff, E.2    Deubzer, B.3    Witke, W.4    Gerisch, G.5    Sackmann, E.6
  • 68
    • 0026860948 scopus 로고
    • Dynamics of the Dictyostelium cytoskeleton during chemotaxis
    • Schleicher, M., and A.A. Noegel. 1992. Dynamics of the Dictyostelium cytoskeleton during chemotaxis. The New Biologist. 4:461-472.
    • (1992) The New Biologist , vol.4 , pp. 461-472
    • Schleicher, M.1    Noegel, A.A.2
  • 69
    • 0024015069 scopus 로고
    • A Dictyostelium mutant with severe defects in α-actinin: Its characterization using cDNA probes and monoclonal antibodies
    • Schleicher, M., A.A. Noegel, T. Schwarz, E. Wallraff, M. Brink, J. Faix, G. Gerisch, and G. Isenberg. 1988. A Dictyostelium mutant with severe defects in α-actinin: its characterization using cDNA probes and monoclonal antibodies. J. Cell Sci. 90:59-71.
    • (1988) J. Cell Sci. , vol.90 , pp. 59-71
    • Schleicher, M.1    Noegel, A.A.2    Schwarz, T.3    Wallraff, E.4    Brink, M.5    Faix, J.6    Gerisch, G.7    Isenberg, G.8
  • 70
    • 0023127382 scopus 로고
    • Selection of chemotaxis mutants of Dictyostelium discoideum
    • Segall, J.E., P.R. Fisher, and G. Gerisch. 1987. Selection of chemotaxis mutants of Dictyostelium discoideum. J. Cell Biol. 104:151-161.
    • (1987) J. Cell Biol. , vol.104 , pp. 151-161
    • Segall, J.E.1    Fisher, P.R.2    Gerisch, G.3
  • 71
    • 0029045856 scopus 로고
    • Strain-dependent epithelial defects in mice lacking the EGF receptor
    • Sibilia, M., and E.F. Wagner. 1995. Strain-dependent epithelial defects in mice lacking the EGF receptor. Science (Wash. DC). 269:234-238.
    • (1995) Science (Wash. DC) , vol.269 , pp. 234-238
    • Sibilia, M.1    Wagner, E.F.2
  • 73
    • 0027278479 scopus 로고
    • Two developmentally regulated mRNAs encoding actin-binding proteins in Physarum polycephalum
    • St.-Pierre, B., C. Couture, A. Larouche, and D. Pallotta. 1993. Two developmentally regulated mRNAs encoding actin-binding proteins in Physarum polycephalum. Biochim. Biophys. Acta. 1173:107-110.
    • (1993) Biochim. Biophys. Acta , vol.1173 , pp. 107-110
    • St.-Pierre, B.1    Couture, C.2    Larouche, A.3    Pallotta, D.4
  • 74
    • 0030160592 scopus 로고    scopus 로고
    • Control and integration of cell signaling pathways during C. elegans vulval development
    • Sundaram, M., and M. Han. 1996. Control and integration of cell signaling pathways during C. elegans vulval development. BioEssays. 18:473-480.
    • (1996) BioEssays , vol.18 , pp. 473-480
    • Sundaram, M.1    Han, M.2
  • 75
    • 0021923854 scopus 로고
    • Phorbol esters and horseradish peroxidase stimulate pinocytosis and redirect the flow of pinocytosed fluid in macrophages
    • Swanson, J.A., B.D. Yirinec, and S.C. Silverstein. 1985. Phorbol esters and horseradish peroxidase stimulate pinocytosis and redirect the flow of pinocytosed fluid in macrophages. J. Cell Biol. 100:851-859.
    • (1985) J. Cell Biol. , vol.100 , pp. 851-859
    • Swanson, J.A.1    Yirinec, B.D.2    Silverstein, S.C.3
  • 76
    • 0018654598 scopus 로고
    • Cytoplasmic structure and contractility in amoeboid cells
    • Taylor, D.L., and J.S. Condeelis. 1979. Cytoplasmic structure and contractility in amoeboid cells. Int. Rev. Cytol. 56:57-144.
    • (1979) Int. Rev. Cytol. , vol.56 , pp. 57-144
    • Taylor, D.L.1    Condeelis, J.S.2
  • 77
    • 0020474957 scopus 로고
    • Cytoplasmic structure and contractility: The solation-contraclion coupling hypothesis
    • Taylor, D.L., and M. Fechheimer. 1982. Cytoplasmic structure and contractility: the solation-contraclion coupling hypothesis. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 299:185-197.
    • (1982) Philos. Trans. R. Soc. Lond. B. Biol. Sci. , vol.299 , pp. 185-197
    • Taylor, D.L.1    Fechheimer, M.2
  • 78
    • 0027382270 scopus 로고
    • Thinking about genetic redundancy
    • Thomas, J.H. 1993. Thinking about genetic redundancy. Trends Genet. 9:395-399.
    • (1993) Trends Genet. , vol.9 , pp. 395-399
    • Thomas, J.H.1
  • 80
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Slaehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Slaehelin, T.2    Gordon, J.3
  • 81
    • 0027162413 scopus 로고
    • Affinity of α-actinin for actin determines the structure and mechanical properties of actin filament gels
    • Wachsstock, D.H., W.H. Schwarz, and T.D. Pollard. 1993. Affinity of α-actinin for actin determines the structure and mechanical properties of actin filament gels. Biophys. J. 65:205-214.
    • (1993) Biophys. J. , vol.65 , pp. 205-214
    • Wachsstock, D.H.1    Schwarz, W.H.2    Pollard, T.D.3
  • 82
    • 0028265522 scopus 로고
    • Cross-linker dynamics determine the mechanical properties of actin gels
    • Wachsstock, D.H., W.H. Schwarz, and T.D. Pollard. 1994. Cross-linker dynamics determine the mechanical properties of actin gels. Biophys. J. 66:801-809.
    • (1994) Biophys. J. , vol.66 , pp. 801-809
    • Wachsstock, D.H.1    Schwarz, W.H.2    Pollard, T.D.3
  • 83
    • 0022603987 scopus 로고
    • Selection of Dictyostelium mutants defective in cytoskeletal proteins: The use of an antibody that binds to the ends of α-actinin rods
    • Wallraff, E., M. Schleicher, M. Modersitzki, D. Rieger, G. Isenberg, and G. Gerisch. 1986. Selection of Dictyostelium mutants defective in cytoskeletal proteins: the use of an antibody that binds to the ends of α-actinin rods. EMBO (Eur. Mol. Biol. Organ.) J. 5:61-67.
    • (1986) EMBO (Eur. Mol. Biol. Organ.) J. , vol.5 , pp. 61-67
    • Wallraff, E.1    Schleicher, M.2    Modersitzki, M.3    Rieger, D.4    Isenberg, G.5    Gerisch, G.6
  • 84
    • 0014841120 scopus 로고
    • Growth of myxamoebae of the cellular slime mould Dictyostelium discoideum in axenic culture
    • Watts, D.J., and J.M. Ashworth. 1970. Growth of myxamoebae of the cellular slime mould Dictyostelium discoideum in axenic culture. Biochem. J. 119: 171-174.
    • (1970) Biochem. J. , vol.119 , pp. 171-174
    • Watts, D.J.1    Ashworth, J.M.2
  • 85
    • 0028916228 scopus 로고
    • Motility and substratum adhesion of Dictyostelium wild-type and cytoskeletal mutant cells: A study by RICM/bright-field double-view image analysis
    • Weber, I., E. Wallraff, R. Albrecht, and G. Gerisch. 1995. Motility and substratum adhesion of Dictyostelium wild-type and cytoskeletal mutant cells: a study by RICM/bright-field double-view image analysis. J. Cell Sci. 108: 1519-1530.
    • (1995) J. Cell Sci. , vol.108 , pp. 1519-1530
    • Weber, I.1    Wallraff, E.2    Albrecht, R.3    Gerisch, G.4
  • 86
    • 0027361181 scopus 로고
    • The actin-binding protein comitin (p24) is a component of the Golgi apparatus
    • Weiner, O.H., J. Murphy, G. Griffiths, M. Schleicher, and A.A. Noegel. 1993. The actin-binding protein comitin (p24) is a component of the Golgi apparatus. J. Cell Biol. 123:23-34.
    • (1993) J. Cell Biol. , vol.123 , pp. 23-34
    • Weiner, O.H.1    Murphy, J.2    Griffiths, G.3    Schleicher, M.4    Noegel, A.A.5
  • 88
    • 0015975959 scopus 로고
    • Genetics of growth in axenic medium of the cellular slime mould Dictyostelium discoideum
    • Williams, K.L., R.H. Kessin, and P.C. Newell. 1974a. Genetics of growth in axenic medium of the cellular slime mould Dictyostelium discoideum. Nature (Lond.). 247:142-143.
    • (1974) Nature (Lond.) , vol.247 , pp. 142-143
    • Williams, K.L.1    Kessin, R.H.2    Newell, P.C.3
  • 89
    • 0016159293 scopus 로고
    • Parasexual genetics in Dictyostelium discoideum: Mitotic analysis of acriflavin resistance and growth in axenic medium
    • Williams, K.L., R.H. Kessin, and P.C. Newell. 1974b. Parasexual genetics in Dictyostelium discoideum: mitotic analysis of acriflavin resistance and growth in axenic medium. J. Gen. Microbiol. 84:59-69.
    • (1974) J. Gen. Microbiol. , vol.84 , pp. 59-69
    • Williams, K.L.1    Kessin, R.H.2    Newell, P.C.3
  • 90
    • 0017282039 scopus 로고
    • A genetic study in the cellular slime mold Dictyostelium discoideum using complementation analysis
    • Williams, K.L., and P.C. Newell. 1976. A genetic study in the cellular slime mold Dictyostelium discoideum using complementation analysis. Genetics. 82:287-307.
    • (1976) Genetics , vol.82 , pp. 287-307
    • Williams, K.L.1    Newell, P.C.2
  • 91
    • 0023661339 scopus 로고
    • Homologous recombination in the Dictyostelium α-actinin gene leads to an altered mRNA and lack of protein
    • Witke, W., W. Nellen, and A.A. Noegel. 1987. Homologous recombination in the Dictyostelium α-actinin gene leads to an altered mRNA and lack of protein. EMBO (Eur. Mol. Biol. Organ.) J. 6:4143-4148.
    • (1987) EMBO (Eur. Mol. Biol. Organ.) J. , vol.6 , pp. 4143-4148
    • Witke, W.1    Nellen, W.2    Noegel, A.A.3
  • 92
    • 0026593102 scopus 로고
    • Redundancy in the microfilament system: Abnormal development of Dictyostelium cells lacking two F-actin cross-linking proteins
    • Witke, W., M. Schleicher, and A.A. Noegel. 1992. Redundancy in the microfilament system: abnormal development of Dictyostelium cells lacking two F-actin cross-linking proteins. Cell. 68:53-62.
    • (1992) Cell , vol.68 , pp. 53-62
    • Witke, W.1    Schleicher, M.2    Noegel, A.A.3
  • 94
    • 0026645917 scopus 로고
    • Inhibition of actin filament depolymerization by the Dictyostelium 30,000-D actin-bundling protein
    • Zigmond, S.H., R. Furukawa, and M. Fechheimer. 1992. Inhibition of actin filament depolymerization by the Dictyostelium 30,000-D actin-bundling protein. J. Cell Biol. 119:559-567.
    • (1992) J. Cell Biol. , vol.119 , pp. 559-567
    • Zigmond, S.H.1    Furukawa, R.2    Fechheimer, M.3


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